Search Results
Overview
| Uniprot ID | Q9P258 |
|---|---|
| Protein Name | Protein RCC2 |
| Gene Name | RCC2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 124 | IGRKEVPKQQAAYRN |
| 293 | LGHNSDGKFIARAQR |
| 5 | ***MPRKKAAAAAWE |
| 77 | ARPATAGKAGGAAVV |
| 92 | ITEPEHTKERVKLEG |
Function
Multifunctional protein that may affect its functions by regulating the activity of small GTPases, such as RAC1 and RALA (PubMed:12919680, PubMed:25074804, PubMed:26158537, PubMed:28869598). Required for normal progress through the cell cycle, both during interphase and during mitosis (PubMed:12919680, PubMed:23388455, PubMed:26158537). Required for the presence of normal levels of MAD2L1, AURKB and BIRC5 on inner centromeres during mitosis, and for normal attachment of kinetochores to mitotic spindles (PubMed:12919680, PubMed:26158537). Required for normal organization of the microtubule cytoskeleton in interphase cells (PubMed:23388455). Functions as guanine nucleotide exchange factor (GEF) for RALA (PubMed:26158537). Interferes with the activation of RAC1 by guanine nucleotide exchange factors (PubMed:25074804). Prevents accumulation of active, GTP-bound RAC1, and suppresses RAC1-mediated reorganization of the actin cytoskeleton and formation of membrane protrusions (PubMed:25074804, PubMed:28869598). Required for normal cellular responses to contacts with the extracellular matrix of adjacent cells, and for directional cell migration in response to a fibronectin gradient (in vitro) (PubMed:25074804, PubMed:28869598)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0034506 | chromosome, centromeric core domain |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0031901 | early endosome membrane |
| Cellular Component | GO:0005874 | microtubule |
| Cellular Component | GO:0030496 | midbody |
| Cellular Component | GO:1990023 | mitotic spindle midzone |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0005085 | guanyl-nucleotide exchange factor activity |
| Molecular Function | GO:0008017 | microtubule binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0031267 | small GTPase binding |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0072356 | chromosome passenger complex localization to kinetochore |
| Biological Process | GO:0045184 | establishment of protein localization |
| Biological Process | GO:0048041 | focal adhesion assembly |
| Biological Process | GO:0007229 | integrin-mediated signaling pathway |
| Biological Process | GO:0051895 | negative regulation of focal adhesion assembly |
| Biological Process | GO:0034260 | negative regulation of GTPase activity |
| Biological Process | GO:1900025 | negative regulation of substrate adhesion-dependent cell spreading |
| Biological Process | GO:0051987 | positive regulation of attachment of spindle microtubules to kinetochore |
| Biological Process | GO:0010971 | positive regulation of G2/M transition of mitotic cell cycle |
| Biological Process | GO:0030334 | regulation of cell migration |
| Biological Process | GO:0010762 | regulation of fibroblast migration |
| Biological Process | GO:1900027 | regulation of ruffle assembly |
Reference
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[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[6] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[7] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[8] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[9] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[10] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[11] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.